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Biomedical subjects

W Gibson

Publications and source records attributed to W Gibson.

At least 145 records · Page 8Linked to original sources
PubMed1981

Pathology of the intrinsic muscles of the larynx.

The intrinsic muscles of the larynx were exposed in each of 54 normal larynges derived from the autopsy series of a general hospital and submitted to microscopic examination. Muscle fibre alterations were found in all the posterior cricocarytenoid muscles in patients from 13 years of age on wards. In about half of the patients these changes included necrosis of segments of muscle fibres and secondary cellular reactions to this. In two cases of chronic autonomic failure with multiple system atrophy the intrinsic laryngeal muscles were similarly examined. Both cases showed a marked gross and microscopic atrophy of the posterior cricoarytenoid muscles; there were also microscopic changes similar to those found in the normal population. The significance of the changes in the routine post-mortem larynges, the changes in the cases of chronic autonomic failure with multiple system atrophy and the relationship between the two are discussed.

Adolescent↗
PubMed1979

Syringing the ear.

Explore the source record for details and available documents.

Ear Diseases↗
PubMed1979

Polyoma viruses with mutations at endonuclease HindII site 1: alterations at the COOH terminus of VP1.

Four mutants of polyoma virus lacking endonuclease HindII site 1 were isolated and characterized with respect to the VP1 coding sequence. Three of these mutants had deletions that removed 0.2 to 0.3% of the genome. All three deletion mutants encoded VP1 proteins that were smaller than wild type and that lacked one or more tryptic peptides normally found in the wild-type VP1 protein. Our results suggest the HindII site 1 is at, or very near, the carboxy terminal end of the coding sequence for VP1. A model for the peptide organization in that region is presented.

Capsid↗
PubMed1978

Characterization of the mRNA's for the polyoma virus capsid proteins VP1, VP2, and VP3.

Polyadenylated cytoplasmic RNA from polyoma virus-infected cells can be translated in the wheat germ system to yield all there polyoma virus capsid proteins, VP1, VP2, and VP3. The translation products of RNA selected from total cytoplasmic RNA of infected cells by hybridization to polyoma virus DNA showed a high degree of enrichment for VP1, VP2, and VP3. The identity of the in vitro products with authentic virion proteins was established in two ways. First, tryptic peptide maps of the in vitro products were found to be essentially identical to those of their in vivo counterparts. Second, the mobilities of the in vitro products on two-dimensional gels were the same as those of viral proteins labeled in vivo. VP1, VP2, and vp3 were all labeled with [35S] formylmethionine when they were synthesized in the presence of [35S] formylmethionyl-tRNAfmet. We determined the sizes of the polyadenylated mRNA's for VP1, VP2, and VP3 by fractionation on gels. The sizes of the major mRNA species for the capsid proteins are as follows: VP2, 8.5 X 10(5) daltons; VP3, 7.4 X 10(5) daltons; and VP1, 4.6 X 10(5) daltons. We conclude that all three viral capsid proteins are synthesized independently in vitro, that all three viral capsid proteins are virally coded, and that each of the capsid proteins has a discrete mRNA.

Capsid↗
PubMed1978

The identification of Trypanosoma brucei gambiense in Liberian pigs and dogs by isoenzymes and by resistance to human plasma.

29 Trypanozoon stocks from Liberian pigs and dogs were screened for human plasma resistance and electrophoretic isoenzyme patterns of eleven enzymes. Two stocks from pigs were found both to be resistant to human plasma and to have an isoenzyme marker, a slow alanine aminotransferase (ALAT) pattern, previously found only in Trypanosoma brucei gambiense from man. This constitutes evidence that the pig is a reservoir of human trypanosomiasis in West Africa. The T.b.gambiense ALAT was also found in stocks from 5 other pigs and a dog, but none of these stocks was resistant to human plasma; conversely, 9 further isolations from pigs and 2 from dogs were plasma resistant but did not have the T.b.gambiense ALAT. The lack of correspondence between the two characteristics is discussed. A T.b.gambiense stock from man in Zaire had the ALAT pattern characteristic of T.b.gambiense from Senegal and Nigeria, together with the ASAT triplet found in most T.b.gambiense stocks. Peptidase polymorphism was shown in trypanosomes for the first time.

Alanine Transaminase↗
PubMed1976

Identification and characterization of multiple forms of actin.

Multiple forms of actin have been found in a variety of mammalian cell lines and tissues by the use of high resolution, two-dimensional gel electrophoresis. One form (alpha actin) was found only in differentiated muscle cells, and its synthesis is induced during myogenesis in culture. Two other forms (beta and gamma actin) are present in all nonmuscle cell types examined, and they continue to be synthesized in cultured muscle cells after fusion. Tryptic peptide comparisons have shown that muscle actin is distinguished from the two "nonmuscle" actins by several peptide differences, and that the two non-muscle actins are nearly identical. All three forms contain equimolar amounts of N-methylhistidine, and extensive controls have shown no evidence of artifactual heterogeneity. In addition to the three major actins, two other proteins were identified as probably forms of actin by affinity for DNAase I-agarose. These proteins are similar in charge and molecular weight to the major actin forms, but are unstable and have lifetimes in the cell of less than 2 hr.

Actins↗
PubMed1974

Studies on the reverse transcriptase of RNA tumor viruses. Structural relatedness of two subunits of avian RNA tumor viruses.

The structural relationship of the small (alpha) and large (beta) subunits of reverse transcriptase isolated from two avian RNA tumor viruses has been examined by tryptic peptide analysis. Comparison of the tryptic hydrolysates of the isolated subunits by two-dimensional separation on thin-layer cellulose plates indicates that (i) the alpha subunit of reverse transcriptase of avian myeloblastosis virus is structurally related to the beta subunit; (ii) the alpha and beta subunits of the enzyme of Rous sarcoma virus also appear to be related; and (iii) there appears to be an extensive amino-acid sequence homology between reverse transcriptases of avian myeloblastosis virus and Rous sarcoma virus. Evidence is also presented that both alpha and beta subunits can be identified in purified avian myeloblastosis virions.

Amino Acid Sequence↗
PubMed1974

Proteins specified by herpes simplex virus. Staining and radiolabeling properties of B capsid and virion proteins in polyacrylamide gels.

ANALYSES OF THE STRUCTURAL PROTEINS OF HERPES SIMPLEX VIRIONS AND OF CAPSIDS CONTAINING VIRAL DNA (B CAPSIDS), AFTER ELECTROPHORESIS IN POLYACRYLAMIDE GELS, REVEALED CONSIDERABLE VARIABILITY IN THEIR PROPERTIES WITH RESPECT TO: (i) retention of Coomassie brilliant blue (CBB) and fast green stains during destaining, (ii) relative optical absorbance of the CBB-protein complex at different wavelengths, (iii) relative efficiency with which (14)C-amino acids are incorporated during early and late periods of the infection cycle, and (iv) capacity to be phosphorylated in vivo. In addition, it was found that protein 22a of B capsids, which does not have an electrophoretically identical counterpart in virions, shares a relatively unique set of staining and radiolabeling properties with virion protein 22, which has a slightly more rapid electrophoretic mobility in sodium dodecyl sulfate-polyacrylamide gels.

Amino Acids↗
PubMed1972

Proteins specified by herpes simplex virus. 8. Characterization and composition of multiple capsid forms of subtypes 1 and 2.

Two classes of herpesvirus capsids, designated A and B, were isolated from the nuclei of human cells infected with herpes simplex virus (HSV). A and B capsids share in common four structural proteins, i.e., no. 5, 19, 23, and 24. B capsids contain 7.7 to 9.7 times more deoxyribonucleic acid than A capsids; moreover, they contain proteins no. 21 and 22a in addition. All of the proteins contained in the capsid except no. 22a are present in the enveloped nucleocapsids (virions) in approximately the same molar ratios. The capsid proteins of HSV-1 cannot be differentiated from their HSV-2 counterparts with respect to electrophoretic mobility. A third class of capsids, designated C capsids, was isolated from virions contained in the cytoplasm of infected cells by the same procedure used to obtain A and B capsids. The C capsids contain all of the proteins present in A capsids plus proteins 1 to 3 and 21.

Animals↗